2mq1: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 2mq1~~ is ~~ON HOLD~~

==Phosphotyrosine binding domain==

== Structural highlights ==

<table><tr><td colspan='2'>[[2mq1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MQ1 FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mq1 OCA], [https://pdbe.org/2mq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2mq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mq1 ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/HAKAI_MOUSE HAKAI_MOUSE] Promotes ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1. Targets CDH1 for endocytosis and degradation.<ref>PMID:11836526</ref> <ref>PMID:22252131</ref>

== Publication Abstract from PubMed ==

Hakai, an E3 ubiquitin ligase, disrupts cell-cell contacts in epithelial cells and is up-regulated in human colon and gastric adenocarcinomas. Hakai acts through its phosphotyrosine-binding (HYB) domain, which bears a dimeric fold that recognizes the phosphotyrosine motifs of E-cadherin, cortactin, DOK1, and other Src substrates. Unlike the monomeric nature of the SH2 and phosphotyrosine-binding domains, the architecture of the HYB domain consists of an atypical, zinc-coordinated tight homodimer. Here, we report a C-terminal truncation mutant of the HYB domain (HYB(DeltaC)), comprising amino acids 106-194, which exists as a monomer in solution. The NMR structure revealed that this deletion mutant undergoes a dramatic structural change caused by a rearrangement of the atypical zinc-coordinated unit in the C terminus of the HYB domain to a C2H2-like zinc finger in HYB(DeltaC). Moreover, using isothermal titration calorimetry, we show that dimerization of HYB(DeltaC) can be induced using a phosphotyrosine substrate peptide. This ligand-induced dimerization of HYB(DeltaC) is further validated using analytical ultracentrifugation, size-exclusion chromatography, NMR relaxation studies, dynamic light scattering, and circular dichroism experiments. Overall, these observations suggest that the dimeric architecture of the HYB domain is essential for the phosphotyrosine-binding property of Hakai.

~~Authors~~: Mukherjee, M., Jing-Song, F., ~~Jayaraman, S~~.

Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR structure.,Mukherjee M, Jing-Song F, Ramachandran S, Guy GR, Sivaraman J J Biol Chem. 2014 Sep 12;289(37):25611-23. doi: 10.1074/jbc.M114.592840. Epub, 2014 Jul 29. PMID:25074933<ref>PMID:25074933</ref>

~~Description~~: ~~Phosphotyrosine binding domain~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Mus musculus]]

[[Category: Jing-Song F]]

[[Category: Mukherjee M]]

[[Category: Sivaraman J]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2mq1 is ON HOLD
+==Phosphotyrosine binding domain==
+<StructureSection load='2mq1' size='340' side='right'caption='[[2mq1]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2mq1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MQ1 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mq1 OCA], [https://pdbe.org/2mq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2mq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mq1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HAKAI_MOUSE HAKAI_MOUSE] Promotes ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1. Targets CDH1 for endocytosis and degradation.<ref>PMID:11836526</ref> <ref>PMID:22252131</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Hakai, an E3 ubiquitin ligase, disrupts cell-cell contacts in epithelial cells and is up-regulated in human colon and gastric adenocarcinomas. Hakai acts through its phosphotyrosine-binding (HYB) domain, which bears a dimeric fold that recognizes the phosphotyrosine motifs of E-cadherin, cortactin, DOK1, and other Src substrates. Unlike the monomeric nature of the SH2 and phosphotyrosine-binding domains, the architecture of the HYB domain consists of an atypical, zinc-coordinated tight homodimer. Here, we report a C-terminal truncation mutant of the HYB domain (HYB(DeltaC)), comprising amino acids 106-194, which exists as a monomer in solution. The NMR structure revealed that this deletion mutant undergoes a dramatic structural change caused by a rearrangement of the atypical zinc-coordinated unit in the C terminus of the HYB domain to a C2H2-like zinc finger in HYB(DeltaC). Moreover, using isothermal titration calorimetry, we show that dimerization of HYB(DeltaC) can be induced using a phosphotyrosine substrate peptide. This ligand-induced dimerization of HYB(DeltaC) is further validated using analytical ultracentrifugation, size-exclusion chromatography, NMR relaxation studies, dynamic light scattering, and circular dichroism experiments. Overall, these observations suggest that the dimeric architecture of the HYB domain is essential for the phosphotyrosine-binding property of Hakai.
-Authors: Mukherjee, M., Jing-Song, F., Jayaraman, S.
+Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR structure.,Mukherjee M, Jing-Song F, Ramachandran S, Guy GR, Sivaraman J J Biol Chem. 2014 Sep 12;289(37):25611-23. doi: 10.1074/jbc.M114.592840. Epub, 2014 Jul 29. PMID:25074933<ref>PMID:25074933</ref>
-Description: Phosphotyrosine binding domain
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2mq1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Jing-Song F]]
+[[Category: Mukherjee M]]
+[[Category: Sivaraman J]]